Dodecyl-β-melibioside Detergent Micelles as a Medium for Membrane Proteins.

Hutchison JM, Lu Z, Li GC, Travis B, Mittal R, Deatherage CL, Sanders CR
Biochemistry. 2017 56 (41): 5481-5484

PMID: 28980804 · PMCID: PMC5685800 · DOI:10.1021/acs.biochem.7b00810

There remains a need for new non-ionic detergents that are suitable for use in biochemical and biophysical studies of membrane proteins. Here we explore the properties of n-dodecyl-β-melibioside (β-DDMB) micelles as a medium for membrane proteins. Melibiose is d-galactose-α(1→6)-d-glucose. Light scattering showed the β-DDMB micelle to be roughly 30 kDa smaller than micelles formed by the commonly used n-dodecyl-β-maltoside (β-DDM). β-DDMB stabilized diacylglycerol kinase (DAGK) against thermal inactivation. Moreover, activity assays conducted using aliquots of DAGK purified into β-DDMB yielded activities that were 40% higher than those of DAGK purified into β-DDM. β-DDMB yielded similar or better TROSY-HSQC NMR spectra for two single-pass membrane proteins and the tetraspan membrane protein peripheral myelin protein 22. β-DDMB appears be a useful addition to the toolbox of non-ionic detergents available for membrane protein research.

MeSH Terms (19)

Amyloid beta-Protein Precursor Detergents Diacylglycerol Kinase Disaccharides Dynamic Light Scattering Enzyme Stability Escherichia coli Proteins Glucosides Glycolipids Hot Temperature Humans Micelles Myelin Proteins Nuclear Magnetic Resonance, Biomolecular Particle Size Peptide Fragments Protein Interaction Domains and Motifs Protein Stability Receptor, Notch1

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